ID   A0A2K5CS48_AOTNA        Unreviewed;      1049 AA.
AC   A0A2K5CS48;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Ubiquitin like modifier activating enzyme 6 {ECO:0000313|Ensembl:ENSANAP00000011518.1};
GN   Name=UBA6 {ECO:0000313|Ensembl:ENSANAP00000011518.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000011518.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000011518.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673}.
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DR   AlphaFoldDB; A0A2K5CS48; -.
DR   Ensembl; ENSANAT00000029329.1; ENSANAP00000011518.1; ENSANAG00000023689.1.
DR   GeneTree; ENSGT00940000158826; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd01491; Ube1_repeat1; 1.
DR   CDD; cd01490; Ube1_repeat2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR   Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR   Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR   Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR   Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR   InterPro; IPR032420; E1_4HB.
DR   InterPro; IPR032418; E1_FCCH.
DR   InterPro; IPR042302; E1_FCCH_sf.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR018965; Ub-activating_enz_E1_C.
DR   InterPro; IPR042449; Ub-E1_IAD_1.
DR   InterPro; IPR038252; UBA_E1_C_sf.
DR   InterPro; IPR019572; UBA_E1_SCCH.
DR   InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR018075; UBQ-activ_enz_E1.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   NCBIfam; TIGR01408; Ube1; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   PANTHER; PTHR10953:SF186; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 6; 1.
DR   Pfam; PF16191; E1_4HB; 1.
DR   Pfam; PF16190; E1_FCCH; 1.
DR   Pfam; PF09358; E1_UFD; 1.
DR   Pfam; PF00899; ThiF; 2.
DR   Pfam; PF10585; UBA_E1_SCCH; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SMART; SM00985; UBA_e1_C; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020}.
FT   DOMAIN          918..1040
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
SQ   SEQUENCE   1049 AA;  118244 MW;  2DE95B1B4F849826 CRC64;
     SFNSFFVLFF PPEEESCSCR PDCTNKNLPI MSTASVEIDD ALYSRQRYVL GDTAMQKMAK
     SHVFLSGMGG LGLEIAKNLV LAGIKAVTIH DTEKCRAWDL GTNFFLSEDD IVNKRNRAEA
     VLKHIAELNP YVHVTSSSVP FNETTDLSFL DKYQCVVLTE MELSLQKMIN DFCRSQCPPI
     KFISADVHGI WSRLFCDFGD EFEVLDTTGE EPKEIFISNI TQANPGIVTC LENHPHKLET
     GQFLTFREIN GMTGLNGSIQ QITVISPFSF SIGDTTELEP YLHGGIAVQV KTPKIFCFEP
     LERQIKHPKC LIVDFSKPEA PLEIHTAMLA LDQFQEKYNR KPNVGCQKDS EELLKLATSI
     SETLEEKPDV NADIVHWLSW TAQGFLSPLA AAVGGVASQE VLKAVTGKFS PLCQWLYLEA
     ADIVESLGKP ECEEFLPRGD RYDALRACIG DTLCQKLQNL NIFLVGCGAI GCEMLKNFAL
     LGVGTSKDKG MVTVTDPDLI EKSNLNRQFL FRPHHIQKPK SYTAADATLK INPQIKIDAH
     LNKVCPATET IYNDEFYTKQ DIIVTALDNV EARRYVDSRC LANLRPLLDS GTMGTKGHTE
     VIVPHLTESY NSHRDPPEEE IPFCTLKSFP AAIEHTIQWA RDKFESSFSH KPSLFNKFWQ
     TYSSAEEVLQ KIQSGHSLEG CFQVIKLLSR RPRNWSQCVE LARLKFEKYF NHKALQLLHC
     FPLDIRLKDG SNIVFKTLHS NFALFFNFKR HLSFLQNAAK LYATVYCIPF TEEDLSADAL
     LNILSEVKIQ EFKPSNKVVQ TDETARKPDH VPISNEDERN AIFQLEKAIL SNEATKSDLQ
     MAVLSFEKDD DRNGHIDFIT AASNLRAKMY NIEPADRFKT KRIAGKIIPA IATTTATVSG
     LVALEVIKVT GGYPFEAYKN CFLNFAIPII VFTETSEVRK TKIRNGISFT IWDRWTVHGK
     EDFTLLDFIN AVKEKYGIEP TMVVQGVKML YVPVMPGHAK RLKLTMHKLV KPSTEKKYVD
     LTVSFAPDID GDEDLPGPPV RYYFSHDTD
//